Oncogenic signaling downstream of NRASD12 is disrupted by blocking palmitoylation. Serum-starved lysates of NIH3T3 cells expressing vector, NRASD12, NRASD12^C181S, or NRASD12^C186S were analyzed by Western blotting. (A) Effect of palmitoylation and prenylation of NRASD12 on phosphorylation of Akt and S6 ribosomal protein. (B) Effect of palmitoylation and prenylation of NRASD12 on phosphorylation of Erk. (C) Effect of palmitoylation and prenylation of NRASD12 on Ral activation. Ral-GTP precipitated from serum-starved NIH3T3 cells expressing vector control, NRASD12, NRASD12^C181S, or NRASD12^C186S with GST-RalBP1 glutathione agarose beads with or without addition of GTPγS were analyzed by Western blotting with an anti-RalA antibody. Input RalA was also probed. RAS expression was detected as a loading control.